Evidence map›Paper›PMID 25006873›Full record

ArticleNature communications2014

Taking snapshots of photosynthetic water oxidation using femtosecond X-ray diffraction and spectroscopy.

Jan Kern, Rosalie Tran, Roberto Alonso-Mori, Sergey Koroidov, Nathaniel Echols, Johan Hattne, Mohamed Ibrahim, Sheraz Gul, Hartawan Laksmono, Raymond G Sierra and 32 more

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
16.2field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

102 citing papers in PubMed, 230 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Cryo-EM meets crystallography: A model-independent view of the heteronuclear MnProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Competitive interaction of Mn(II) and Fe(II) cations with the high-affinity Mn-binding site of the photosystem II: evolutionary aspect.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2022
    Article
  19. Serial femtosecond crystallography.Nature reviews. Methods primers · 2022
    Article
  20. Article

42 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

42 authors at 9 institutions in 4 countries.

Jan Kern1] Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA [2] LCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Rosalie TranPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Roberto Alonso-MoriLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Sergey KoroidovInstitutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, 90187 Umeå, Sweden.
Nathaniel EcholsPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Johan HattnePhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Mohamed Ibrahim1] Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany [2] Max-Volmer-Laboratorium für Biophysikalische Chemie, Technische Universität, D-10623 Berlin, Germany.
Sheraz GulPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Hartawan LaksmonoPULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Raymond G SierraPULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Richard J Gildea1] Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA [2].
Guangye HanPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Julia Hellmich1] Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany [2] Max-Volmer-Laboratorium für Biophysikalische Chemie, Technische Universität, D-10623 Berlin, Germany.
Benedikt Lassalle-Kaiser1] Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA [2].
Ruchira ChatterjeePhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Aaron S BrewsterPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Claudiu A StanPULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Carina GlöcknerMax-Volmer-Laboratorium für Biophysikalische Chemie, Technische Universität, D-10623 Berlin, Germany.
Alyssa LampePhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Dörte DiFioreMax-Volmer-Laboratorium für Biophysikalische Chemie, Technische Universität, D-10623 Berlin, Germany.
Despina MilathianakiLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Alan R FryLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
M Marvin Seibert1] LCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA [2].
Jason E KoglinLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Erik GalloEuropean Synchrotron Radiation Facility, F-38043 Grenoble, France.
Jens UhligEuropean Synchrotron Radiation Facility, F-38043 Grenoble, France.
Dimosthenis SokarasSSRL, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Tsu-Chien WengSSRL, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Petrus H ZwartPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
David E SkinnerNational Energy Research Scientific Computing Center, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Michael J Bogan1] LCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA [2] PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Marc MesserschmidtLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Pieter GlatzelEuropean Synchrotron Radiation Facility, F-38043 Grenoble, France.
Garth J WilliamsLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Sébastien BoutetLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Paul D AdamsPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Athina Zouni1] Institut für Biologie, Humboldt-Universität zu Berlin, D-10099 Berlin, Germany [2] Max-Volmer-Laboratorium für Biophysikalische Chemie, Technische Universität, D-10623 Berlin, Germany.
Johannes MessingerInstitutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, 90187 Umeå, Sweden.
Nicholas K SauterPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Uwe BergmannLCLS, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA.
Junko YanoPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Vittal K YachandraPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Lawrence Berkeley National Laboratory · USStanford University · USSLAC National Accelerator Laboratory · USEuropean Synchrotron Radiation Facility · FRTechnische Universität Berlin · DEHumboldt-Universität zu Berlin · DEStanford Synchrotron Radiation Lightsource · USUmeå University · SENational Energy Research Scientific Computing Center · US

Funding

PROJECT 5 - DUKE - STRUCTURE VALIDATION AND IMPROVEMENT FOR PROTEINS AND N. ACIDSP01GM063210 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ADAMS, PAUL DAVID · 2001 to 2021
$33.5M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Taking Snapshots of the Water-Oxidation Reaction by the Mn4Ca Oxygen-Evolving Complex Using X-ray Crystallography and SpectroscopyR01GM055302 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI YACHANDRA, VITTAL · 1997 to 2022
$9.1M
Biological Spectroscopy and Crystallography Using an X-ray Free Electron Laser - Supplemental EquipmentR01GM110501 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Junko Yano · 2014 to 2026
$4.8M
Realizing New Horizons in X-ray Crystallography Data ProcessingR01GM095887 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI SAUTER, NICHOLAS K · 2011 to 2014
$1.5M
Towards real-time XFEL data reduction with CCTBXR01GM102520 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI SAUTER, NICHOLAS K · 2012 to 2015
$1.4M
Structure and Function of the Mn Oxygen-Evolving ComplexR56GM055302 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI YACHANDRA, VITTAL · 2009 to 2009
$530k
NIGMS NIH HHS GM055302NIGMS NIH HHS GM095887NIGMS NIH HHS GM102520NIGMS NIH HHS P01 GM063210NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM055302NIGMS NIH HHS R01 GM095887NIGMS NIH HHS R01 GM102520NIGMS NIH HHS R01 GM110501NIGMS NIH HHS R56 GM055302
6 · The paper itself

Abstract

The dioxygen we breathe is formed by light-induced oxidation of water in photosystem II. O2 formation takes place at a catalytic manganese cluster within milliseconds after the photosystem II reaction centre is excited by three single-turnover flashes. Here we present combined X-ray emission spectra and diffraction data of 2-flash (2F) and 3-flash (3F) photosystem II samples, and of a transient 3F' state (250 μs after the third flash), collected under functional conditions using an X-ray free electron laser. The spectra show that the initial O-O bond formation, coupled to Mn reduction, does not yet occur within 250 μs after the third flash. Diffraction data of all states studied exhibit an anomalous scattering signal from Mn but show no significant structural changes at the present resolution of 4.5 Å. This study represents the initial frames in a molecular movie of the structural changes during the catalytic reaction in photosystem II.

Indexed as

CyanobacteriaModels, ChemicalOxidation-ReductionOxygenPhotosynthesisPhotosystem II Protein ComplexSpectrometry, X-Ray EmissionWaterX-Ray DiffractionOxygenPhotosystem II Protein ComplexWater

Identifiers

PMID25006873
PMCPMC4151126
OpenAlexW2089337437

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.